Structure, regulation, and host interaction of outer membrane protein U (OmpU) of Vibrio species. (January 2022)
- Record Type:
- Journal Article
- Title:
- Structure, regulation, and host interaction of outer membrane protein U (OmpU) of Vibrio species. (January 2022)
- Main Title:
- Structure, regulation, and host interaction of outer membrane protein U (OmpU) of Vibrio species
- Authors:
- Ganie, Hilal A.
Choudhary, Aaina
Baranwal, Somesh - Abstract:
- Abstract: OmpU is a multimeric, cation selective outer membrane protein of Vibrio and related species that non-covalently interact with peptidoglycan layer. Interaction of OmpU with human host cells triggers signaling pathways to promote cytokine secretion, reactive oxygen species production, and caspase independent death in immune and epithelial cells. Non-choleric OmpU imparts resistance to antimicrobial peptides and induces actin cytoskeletal reorganization in the host cells. Further, OmpU isolated from Vibrio species elicits an immune response in several aquaculture hosts. Importantly, in-vivo studies using recombinant OmpU or OmpU derived mimotopes reveal a short-lasting immunity, and protection against Vibrio in the aquaculture sector. In conclusion, OmpU is a key adhesion protein and an important virulence factor for successful colonization of Vibrio species into hosts. This review article provides a broad overview of structural, regulatory, and functional mechanisms of OmpU in normal and disease states. Highlights: ● O uter M embrane P roteins (OMPs) are important adhesion factors that play a role in host colonization and evasion of host defense. ● OmpU, the most abundant and conserved outer membrane protein among Vibrio species, induces proinflammatory response and apoptosis in host cells. ● OmpU activates receptor-mediated pathways in several target cells and enters the cell via clathrin dependent endocytosis. ● OmpU, a strong immunogen, has a potential to protectAbstract: OmpU is a multimeric, cation selective outer membrane protein of Vibrio and related species that non-covalently interact with peptidoglycan layer. Interaction of OmpU with human host cells triggers signaling pathways to promote cytokine secretion, reactive oxygen species production, and caspase independent death in immune and epithelial cells. Non-choleric OmpU imparts resistance to antimicrobial peptides and induces actin cytoskeletal reorganization in the host cells. Further, OmpU isolated from Vibrio species elicits an immune response in several aquaculture hosts. Importantly, in-vivo studies using recombinant OmpU or OmpU derived mimotopes reveal a short-lasting immunity, and protection against Vibrio in the aquaculture sector. In conclusion, OmpU is a key adhesion protein and an important virulence factor for successful colonization of Vibrio species into hosts. This review article provides a broad overview of structural, regulatory, and functional mechanisms of OmpU in normal and disease states. Highlights: ● O uter M embrane P roteins (OMPs) are important adhesion factors that play a role in host colonization and evasion of host defense. ● OmpU, the most abundant and conserved outer membrane protein among Vibrio species, induces proinflammatory response and apoptosis in host cells. ● OmpU activates receptor-mediated pathways in several target cells and enters the cell via clathrin dependent endocytosis. ● OmpU, a strong immunogen, has a potential to protect non-choleric infection in the aquaculture sector. … (more)
- Is Part Of:
- Microbial pathogenesis. Volume 162(2022)
- Journal:
- Microbial pathogenesis
- Issue:
- Volume 162(2022)
- Issue Display:
- Volume 162, Issue 2022 (2022)
- Year:
- 2022
- Volume:
- 162
- Issue:
- 2022
- Issue Sort Value:
- 2022-0162-2022-0000
- Page Start:
- Page End:
- Publication Date:
- 2022-01
- Subjects:
- Virulence -- Innate immunity -- Disease progression -- Vaccine -- NFκB
Pathogenic microorganisms -- Periodicals
Pathology, Molecular -- Periodicals
Communicable Diseases -- microbiology -- Periodicals
Communicable Diseases -- parasitology -- Periodicals
Micro-organismes pathogènes -- Périodiques
Pathologie moléculaire -- Périodiques
Electronic journals
616.9041 - Journal URLs:
- http://www.sciencedirect.com/science/journal/08824010 ↗
http://firstsearch.oclc.org ↗
http://firstsearch.oclc.org/journal=0882-4010;screen=info;ECOIP ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.micpath.2021.105267 ↗
- Languages:
- English
- ISSNs:
- 0882-4010
- Deposit Type:
- Legaldeposit
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- Available online (eLD content is only available in our Reading Rooms) ↗
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- British Library DSC - 5756.955000
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